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Information on EC 5.4.2.8 - phosphomannomutase
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5.4.2.8 phosphomannomutaseIUBMB Comments
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
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Word Map
- 5.4.2.8
-
carbohydrate-deficient
- transferrin
- gdp-mannose
-
multisystemic
-
cdg-ia
-
team
- mannose-1-phosphate
-
pectoralis
- phosphoglucomutase
-
doctors
-
obstetric
-
hypoglycosylation
-
nipple
-
lipid-linked
-
psoas
-
premammillary
-
strabismus
- paromomycin
-
meniscectomy
- medicine
- food industry
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
pmm, phosphomannomutase, orf17, phosphomannomutase 2, phosphomannomutase2, alpha-d-phosphohexomutase, phosphomannose mutase, alpha-phosphomannomutase1, pmm-1, pmm-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.7.5.7
-
-
formerly
-
ORF17
-
-
-
-
PGM/PMM
PGM2
-
Giardia has two proteins with phosphoglucomutase activity, one of which (PGM2) also has phosphomannomutase activity
phosphoglucomutase/phosphomannomutase
Phosphohexomutase
phosphomannomutase
phosphomannomutase 1
phosphomannomutase/phosphoglucomutase
Phosphomannose mutase
-
-
-
-
Phosphomutase, mannose
-
-
-
-
PMM
PMM-A1
PMM-A2
PMM-D1
PMM-D2
PMM/PGM
PMM1
PMM2
PMMH-22
-
-
-
-
SP-2
SSO0207
PMM
-
-
-
-
SP-2
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase activities
SP-2
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase activities
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme
-
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
-
-
-
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
the cosubstrate glucose-1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
the cosubstrate glucose-1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
enzyme is activated by transfer of a phosphate group from mannose-1,6-diphosphate
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
isomerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannose 1,6-phosphomutase
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
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CAS REGISTRY NUMBER
COMMENTARY
59536-73-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose-1-phosphate
D-fructose-6-phosphate
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
-
low enzyme activity
-
-
?
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
-
no mutase activity
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
the interconversion occurs via a mannose-1,6-(bis) phosphate intermediate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
best substrate
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
-
bifunctional enzyme
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
the cosubstrate glucose-1,6-diphosphate or mannose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
the cosubstrate glucose-1,6-diphosphate or mannose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate or mannose 1,6-diphosphate
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
more slowly in the reverse direction
-
?
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
first enzyme of the N-glycosylation pathway
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
D-mannose-1-phosphate
D-mannose-6-phosphate
-
bifunctional enzyme
-
-
?
additional information
?
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
-
PMM1 is less specific: it has nearly equal phosphomannomutase and phosphoglucomutase activities as well as a modest glucose-1,6-bisphosphatase activity corresponding to about 3% of its phosphomannomutase activity
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
first enzyme of the N-glycosylation pathway
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
additional information
Co2+
-
72% of the activation relative to Mg2+, maximal activity at 0.5 mM
Co2+
-
divalent cation required, at 2.0 mM 57% of the activation relative to Mg2+
Mn2+
-
divalent cation required, at 2.0 mM 7% of the activation relative to Mg2+
Ni2+
-
36% of the activation relative to Mg2+, maximal activity at 0.5 mM
Ni2+
-
divalent cation required, at 2.0 mM 22% of the activation relative to Mg2+
additional information
-
no detectable activity after addition of 0.1 mM EDTA
additional information
-
Ni2+, Mn2+ and Zn2+ at a concentration of 1 mM can also support activity, although to a lesser extent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
glucose 6-phosphate
-
poor, competitive with respect to mannose 6-phosphate
IMP
-
IMP stimulates by more than 100fold the intrinsic glucose-1,6-bisphosphatase activity of recombinant PMM1 while inhibiting its phosphoglucomutase activity
inosine monophosphate
inhibits competitively the mutase activity of isoform PMM1
serum- and glucocorticoid-regulated kinase
-
Sgk1 decreases the enzymatic activity of PMM2 in the basal state and upon insulin stimulation in intact COS-7 cells
-
mannose 1-phosphate
-
at high concentrations, competitive with respect to glucose-1,6-diphosphate, Ki: 1.2 mM
additional information
-
not inhibited by Mg2+, D-glucose 6-phosphate, and EDTA
-
additional information
not inhibited by neridronate; not inhibited by neridronate
-
additional information
not inhibited by neridronate; not inhibited by neridronate
-
additional information
-
not inhibited by neridronate; not inhibited by neridronate
-
additional information
-
not inhibitory: 1,5-diamino-4,8-dihydroxyanthraquinone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
inosine monophosphate
the phosphatase activity of isoform PMM1 is enhanced by inosine monophosphate
Insulin
-
incubation with insulin for 45min led to a more than twofold activation of the enzyme
-
alpha-D-glucose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-glucose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-Mannose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from mannose 1,6-diphosphate
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
D-Glucose 1,6-bisphosphate
in presence of 0.02 and 0.2 mM mannose 1-phosphate substrate, half-maximal stimulation of recombinant enzyme at 0.004 and 0.008 mM D-glucose 1,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as mannose 1,6-bisphosphate in activation
D-Mannose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as glucose 1,6-bisphosphate in activation, half-maximal activation in the presence of 0.01 mM and 0.1 mM at 0.0005 mM and 0.001 mM mannose 1,6-bisphosphate, respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37°C
-
0.0073
alpha-D-glucose 1-phosphate
isoform PMM1, at pH 7.5 and 32°C
0.0082
alpha-D-glucose 1-phosphate
isoform PMM2, at pH 7.5 and 32°C
0.0272
alpha-D-glucose 1-phosphate
wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0354
alpha-D-glucose 1-phosphate
mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0366
alpha-D-glucose 1-phosphate
mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0489
alpha-D-glucose 1-phosphate
mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0491
alpha-D-glucose 1-phosphate
mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0493
alpha-D-glucose 1-phosphate
mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0518
alpha-D-glucose 1-phosphate
mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0667
alpha-D-glucose 1-phosphate
mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.4516
alpha-D-glucose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
0.0056
alpha-D-mannose 1-phosphate
-
in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.0065
alpha-D-mannose 1-phosphate
isoform PMM1, at pH 7.5 and 32°C
0.0237
alpha-D-mannose 1-phosphate
isoform PMM2, at pH 7.5 and 32°C
0.1569
alpha-D-mannose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
0.4
alpha-D-mannose 1-phosphate
isoform PMM-D1, 30°C, pH not specified in the publication
0.46
alpha-D-mannose 1-phosphate
isoform PMM-A1, 37°C, pH not specified in the publication
0.48
alpha-D-mannose 1-phosphate
isoform PMM-D2, 30°C, pH not specified in the publication
0.68
alpha-D-mannose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
alpha-D-glucose 1-phosphate
mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.05
alpha-D-glucose 1-phosphate
mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.48
alpha-D-glucose 1-phosphate
mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.87
alpha-D-glucose 1-phosphate
mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.02
alpha-D-glucose 1-phosphate
mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.23
alpha-D-glucose 1-phosphate
mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
2.17
alpha-D-glucose 1-phosphate
mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
7.83
alpha-D-glucose 1-phosphate
wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
82.93
alpha-D-glucose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
2.28
alpha-D-mannose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
134.9
alpha-D-mannose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.35
alpha-D-mannose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
using alpha-D-mannose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
additional information
additional information
-
isoenzyme PH0923S101A PMM Vmax not detectable, 37°C
additional information
-
2-deoxyribose-1-phosphate Vmax 0.230, 90°C
additional information
-
D-glucose-1-phosphate Vmax 0.690, 90°C, pH 7.0
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.5 - 7
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
about 3% activity at pH 3.0-4.0, about 10% activity at pH 5.0, about 80% activity at pH 6.0, 100% activity at pH 7.5, about 30% activity at pH 8.0, about 10% activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
-
about 10% activity at 10°C, about 30% activity at 20°C, about 60% activity at 25°C, about 80% activity at 30°C, 100% activity at 35°C, about 35% activity at 40°C, about 10% activity at 50°C
30 - 37
30 - 37
-
the enzyme activity level is reduced by nearly 95% as the temperature increases from 30 to 37°C
30 - 37
-
the isoform PMM-1 activity level decreases sharply (by more than 90%) as the temperature shifts from 30 to 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
human liver enzyme and recombinant PMM1 from individuals with carbohydrate-deficient glycoprotein syndrome type I
-
-
brenda
isoform PMM-A1; cultivars Xiaoyan 54 and Chinese Spring
C8CK06
UniProt
brenda
isoform PMM-D1; cultivars Xiaoyan 54 and Chinese Spring
UniProt
brenda
isoform PMM-D2; cultivars Xiaoyan 54 and Chinese Spring
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
enzyme is constitutively expressed in both vegetative and reproductive organs
brenda
additional information
-
enzyme is constitutively expressed in both vegetative and reproductive organs
brenda
additional information
quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms
brenda
additional information
-
quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms
brenda
additional information
-
quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
alpha-phosphomannomutase1 is required for GDP-mannose and dolichol-phosphate-mannose biosynthesis
physiological function
additional information
evolution
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
evolution
-
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
-
physiological function
phosphomannomutase is important in the direct or/and indirect control of antibiotic production
physiological function
-
the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
physiological function
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphoacetylglucosamine mutase, EC 5.4.2.3, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
physiological function
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
physiological function
-
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphoacetylglucosamine mutase, EC 5.4.2.3, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
physiological function
-
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
-
additional information
-
analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution
additional information
the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains
additional information
-
the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains
additional information
-
the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains
-
Show AA Sequence and Transmembrane Helices (13631 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
30000
31100
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
active form of PMM/PGM is phosphorylated at Ser108
phosphoprotein
-
mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue, so that activity is reduced only 20fold from that of wild-type
phosphoprotein
-
phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme
phosphoprotein
the enzyme requires conserved phosphoserine 108 for activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform alpha-PMM1 in the open conformation, with and without bound substrate alpha-D-mannose 1-phosphate. Protein consists of two domains, the cap and the core. Substrate phosphate group is at a positively charged site of the cap domain, suggesting that substrate binds first to the cap and then is swept into the active site, thereby facilitating its closure over the core domain
free enzyme and in complex with glucose 1,6-bisphosphate at 2.1 and 2.9 A resolution, resp. Comparison with structure of human enzyme
12-15 mg/ml PMM/PGM solution in 10 mM MOPS, crystals grow by hanging-drop vapor diffusion from 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5 from drops containing 0.002 ml protein and 0.002 ml of well buffer, crystals diffract to 1.75 A
-
crystal structure of the selenomethionine-substituted PMM/PGM at 2.2 A resolution, crystal structure of S108A mutant at 1.75 A resolution
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
purified recombinant detagged enzyme, hanging drop vapour diffusion, from 2 M (NH4)2SO4, 0.2 M NaCl, 0.1 M sodium cacodylate, pH 6.0, 20°C, X-ray diffraction structure determination and analysis at 1.86 A resolution, molecular replacement using a modified form of the Leishmania mexicana enzyme, PDB ID 2i54
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G7R/R37Q
-
temperature-sensitive Arabidopsis thaliana PMM-12 mutant (G7R/R37Q) has lower PMM protein and enzyme activity levels than the wild type enzyme
C241S
the mutant shows 60% residual activity the mutation is associated with phosphomannomutase 2 deficiency
D188G |
mutant of isoform PMM2, 2% of wild-type activiy, involved in congential disorder of glycosylation type 1a
D209G
inactive, the mutation is associated with phosphomannomutase 2 deficiency
D65Y
F119L
F157S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
F207S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
L32R
the mutant shows 45% residual activity the mutation is associated with phosphomannomutase 2 deficiency
P113L
the mutant shows 43% residual activity, the mutation is associated with phosphomannomutase 2 deficiency
P184T
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R123Q
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R141H
R162W
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
T118S
the mutant shows 1% residual activity the mutation is associated with phosphomannomutase 2 deficiency
T237M
the mutant shows 48% residual activity the mutation is associated with phosphomannomutase 2 deficiency
V129M
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
V231M
mutant of isoform PMM2, loss of stability at 40°C, involved in congential disorder of glycosylation type 1a
V44A
the mutant shows 16% residual activity the mutation is associated with phosphomannomutase 2 deficiency
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R20A
R247A
S101A
DELTAmanAB
phosphomannose isomerase, phosphomannosemutase double mutant
additional information
D65Y
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
D65Y
the mutant shows 20% residual activity the mutation is associated with phosphomannomutase 2 deficiency
F119L
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
R141H
mutant of isoform PMM2, 0.4% of wild-type activiy, involved in congential disorder of glycosylation type 1a
R141H
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R141H
the mutation lowers activity to approximately one hundredth of that of wild type enzyme
R247A
-
no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
-
additional information
expression as green fluorescent protein fusion protein in Arabidospsis thaliana increases ascorbic acid content by 25-33%
additional information
-
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
additional information
-
reducing enzyme expression level through virus-induced gene silencing causes substantial decrease in ascorbic acid content in leaves. Raising the expression level leads to 20-50% increase in ascorbic acid content
additional information
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
-
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
-
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
38
-
50% loss of activity within a few min, completely protected from heat inactivation by 1 mM mannose 1-phosphate, 0.01 mM glucose 1,6-diphosphate or 1 mM fructose 1,6-diphosphate. In presence of 1 mM Mg2+: 50% loss of activity after 17 min
100
-
highly stable, half-life of about 85 min in boiling water in presence of 10mM Mg2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange column chromatography, and Sephacryl S-100 gel filtration
-
heat treatment 85°C, 20 min, anion-exchange, hydrophobic and gel filtration column chromatography
-
nickel affinity chromatography column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, removal of the His-tag by TEV protease
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in a temperature-sensitive mutant sec53 yeast strain, expression in BHK cells
-
expression in Escherichia coli
expression in Escherichia coli with His-tag, expression as green fluorescent protein fusion protein in Arabidospsis thaliana
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
-
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene pgmG, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
gene PMM, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli
into the vector pET24ma for transformation of Escherichia coli BL21DE3 cells
-
nucleotide sequence of wild-type and mutant algC genes as well as the transcription and translational initiation sites of the wild-type gene
-
overexpression of histidine-tagged fusion protein in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is up-regulated after treatment with abscisic acid (1.3fold at 0.1 mM), salicylic acid (1.5fold at 0.5 mM), cold (1.7fold at 4°C), polyethylene glycol (1.8fold at 15% (w/v)), and NaCl (1.8fold at 150 mM)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
food industry
medicine
analysis of clinically important mutations involved in congential disorder of glycosylation type 1a
biotechnology
-
enzymatic synthesis of TMP and 2-deoxy-6-phosphate glucose can successfully produce large amount of TDP-2-deoxy-glucose in one-pot by employing phosphomannomutase
biotechnology
the double mutant lacking the PMI and PMM genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins, with further genetic engineering these mutants may activate alternative hexoses as GDP-sugars for transfer to aglycones in vivo
food industry
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
food industry
-
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jaeken, J.; Pirard, M.; Adamowicz, M.; Pronicka, E.; van Schaftingen, E.
Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance
Pediatr. Res.
40
764-766
1996
Homo sapiens
brenda
Small, D.M.; Matheson, N.K.
Phosphomannomutase and phosphoglucomutase in developing Cassia corymbosa seeds
Phytochemistry
18
1147-1150
1979
Cassia corymbosa
-
brenda
Glaser, L.
Phosphomannomutase from yeast
Methods Enzymol.
8
183-185
1966
Saccharomyces cerevisiae
-
brenda
Murata, T.
Purification and some properties of phosphomannomutase from corms of Amorphophallus konjac C. Koch
Plant Cell Physiol.
17
1099-1109
1976
Amorphophallus konjac
-
brenda
Guha, S.K.; Rose, Z.B.
The synthesis of mannose 1-phosphate in brain
Arch. Biochem. Biophys.
243
168-173
1985
Oryctolagus cuniculus
brenda
Padgett, P.J.; Phibbs, P.V.
Phosphomannomutase activity in wild-type and alginate-producing strains of Pseudomonas aeruginosa
Curr. Microbiol.
14
187-192
1986
Pseudomonas aeruginosa
-
brenda
Sa-Correia, I.; Darzins, A.; Wang, S.K.; Berry, A.; Chakrabarty, A.M.
Alginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) gene
J. Bacteriol.
169
3224-3231
1987
Pseudomonas aeruginosa
brenda
Kepes, F.; Schekman, R.
The yeast SEC53 gene encodes phosphomannomutase
J. Biol. Chem.
263
9155-9161
1988
Saccharomyces cerevisiae
brenda
Hansen, S.H.; Frank, S.R.; Casanova, J.E.
Cloning and characterization of human phosphomannomutase, a mammalian homologue of yeast SEC53
Glycobiology
7
829-834
1997
Homo sapiens
brenda
Elling, L.; Ritter, J.E.; Verseck, S.
Expression, purification and characterization of recombinant phosphomannomutase and GDP-alpha-D-mannose pyrophosphorylase from Salmonella enterica, group B, for the synthesis of GDP-alpha-D-mannose from D-mannose
Glycobiology
6
591-597
1996
Salmonella enterica
brenda
Goldberg, J.B.; Hatano, K.; Pier, G.B.
Synthesis of lipopolysaccharide O side chains by Pseudomonas aeruginosa PAO1 requires the enzyme phosphomannomutase
J. Bacteriol.
175
1605-1611
1993
Pseudomonas aeruginosa
brenda
Pirard, M.; Collet, J.F.; Matthijs, G.; van Schaftingen, E.
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
FEBS Lett.
411
251-254
1997
Homo sapiens, Rattus norvegicus
brenda
Oesterhelt, C.; Schnarrenberger, C.; Gross, W.
The reaction mechanism of phosphomannomutase in plants
FEBS Lett.
401
35-37
1997
Galdieria sulphuraria, Embryophyta, Mammalia
brenda
Zielinski, N.A.; Chakrabarty, A.M.; Berry, A.
Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase
J. Biol. Chem.
266
9754-9763
1991
Pseudomonas aeruginosa
brenda
Regni, C.A.; Tipton, P.A.; Beamer, L.J.
Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
56
761-762
2000
Pseudomonas aeruginosa
brenda
Naught, L.E.; Tipton, P.A.
Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Arch. Biochem. Biophys.
396
111-118
2001
Pseudomonas aeruginosa
brenda
Pirard, M.; Achouri, Y.; Collet, J.F.; Schollen, E.; Matthijs, G.; Van Schaftingen, E.
Kinetic properties and tissular distribution of mammalian phosphomannomutase isozymes
Biochem. J.
339
201-207
1999
Homo sapiens, Rattus norvegicus
-
brenda
Popova, T.N.; Matasova, L.V.; Lapot'ko, A.A.
Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves
Biochem. Mol. Biol. Int.
46
461-470
1998
Zea mays
brenda
Naught, L.E.; Regni, C.; Beamer, L.J.; Tipton, P.A.
Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Biochemistry
42
9946-9951
2003
Pseudomonas aeruginosa (P26276)
brenda
Regni, C.; Tipton, P.A.; Beamer, L.J.
Crystal Structure of PMM/PGM: An Enzyme in the Biosynthetic Pathway of P. aeruginosa Virulence Factors
Structure
10
269-279
2002
Pseudomonas aeruginosa (P26276)
brenda
Menniti, M.; Iuliano, R.; Amato, R.; Boito, R.; Corea, M.; Le Pera, I.; Gulletta, E.; Fuiano, G.; Perrotti, N.
Serum and glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells
Am. J. Physiol.
288
C148-155
2005
Homo sapiens
brenda
Liu, H.Y.; Wang, Z.; Regni, C.; Zou, X.; Tipton, P.A.
Detailed kinetic studies of an aggregating inhibitor; inhibition of phosphomannomutase/phosphoglucomutase by disperse blue 56
Biochemistry
43
8662-8669
2004
Pseudomonas aeruginosa
brenda
Rashid, N.; Kanai, T.; Atomi, H.; Imanaka, T.
Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis
J. Bacteriol.
186
6070-6076
2004
Thermococcus kodakarensis
brenda
Akutsu, J.; Zhang, Z.; Tsujimura, M.; Sasaki, M.; Yohda, M.; Kawarabayasi, Y.
Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
J. Biochem.
138
159-166
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Regni, C.; Shackelford, G.S.; Beamer, L.J.
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor
Acta Crystallogr. Sect. F
F62
722-726
2006
Pseudomonas aeruginosa
brenda
Ray, W.K.; Keith, S.M.; DeSantis, A.M.; Hunt, J.P.; Larson, T.J.; Helm, R.F.; Kennelly, P.J.
A phosphohexomutase from the archaeon Sulfolobus solfataricus is covalently modified by phosphorylation on serine
J. Bacteriol.
187
4270-4275
2005
Saccharolobus solfataricus (Q980S1), Saccharolobus solfataricus P2 (Q980S1)
brenda
Silvaggi, N.R.; Zhang, C.; Lu, Z.; Dai, J.; Dunaway-Mariano, D.; Allen, K.N.
The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a
J. Biol. Chem.
281
14918-14926
2006
Homo sapiens (O15305), Homo sapiens (Q92871)
brenda
Regni, C.; Schramm, A.M.; Beamer, L.J.
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme
J. Biol. Chem.
281
15564-15571
2006
Pseudomonas aeruginosa
brenda
Kedzierski, L.; Malby, R.L.; Smith, B.J.; Perugini, M.A.; Hodder, A.N.; Ilg, T.; Colman, P.M.; Handman, E.
Structure of Leishmania mexicana phosphomannomutase highlights similarities with human isoforms
J. Mol. Biol.
363
215-227
2006
Homo sapiens, Leishmania mexicana (Q95ZD7), Leishmania mexicana
brenda
Qian, W.; Yu, C.; Qin, H.; Liu, X.; Zhang, A.; Johansen, I.E.; Wang, D.
Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana
Plant J.
49
399-413
2007
Nicotiana benthamiana, Arabidopsis thaliana (O80840)
brenda
Schramm, A.M.; Mehra-Chaudhary, R.; Furdui, C.M.; Beamer, L.J.
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa
Biochemistry
47
9154-9162
2008
Pseudomonas aeruginosa (P26276)
brenda
Yoon, S.; Park, S.; Kim, Y.; Shin, M.; Chong, C.; Choi, J.
Cloning and characterization of phosphoglucomutase and phosphomannomutase derived from Sphingomonas chungbukensis DJ77
J. Biochem.
144
507-512
2008
Sphingobium chungbukense, Sphingobium chungbukense DJ77
brenda
Veiga-da-Cunha, M.; Vleugels, W.; Maliekal, P.; Matthijs, G.; Van Schaftingen, E.
Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase
J. Biol. Chem.
283
33988-33993
2008
Mus musculus
brenda
Hoeberichts, F.A.; Vaeck, E.; Kiddle, G.; Coppens, E.; van de Cotte, B.; Adamantidis, A.; Ormenese, S.; Foyer, C.H.; Zabeau, M.; Inze, D.; Perilleux, C.; Van Breusegem, F.; Vuylsteke, M.
A temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death
J. Biol. Chem.
283
5708-5718
2008
Arabidopsis thaliana
brenda
Nic Lochlainn, L.; Caffrey, P.
Phosphomannose isomerase and phosphomannomutase gene disruptions in Streptomyces nodosus: impact on amphotericin biosynthesis and implications for glycosylation engineering
Metab. Eng.
11
40-47
2009
Streptomyces nodosus (B6Z254), Streptomyces nodosus
brenda
Badejo, A.A.; Eltelib, H.A.; Fukunaga, K.; Fujikawa, Y.; Esaka, M.
Increase in ascorbate content of transgenic tobacco plants overexpressing acerola (Malpighia glabra) phosphomannomutase gene
Plant Cell Physiol.
50
423-428
2009
Malpighia glabra (C0JP35), Malpighia glabra
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (O80840)
brenda
Yang, Y.H.; Song, E.; Park, S.H.; Kim, J.N.; Lee, K.; Kim, E.; Kim, Y.G.; Kim, B.G.
Loss of phosphomannomutase activity enhances actinorhodin production in Streptomyces coelicolor
Appl. Microbiol. Biotechnol.
86
1485-1492
2010
Streptomyces coelicolor (Q9KZL6), Streptomyces coelicolor
brenda
Yang, Y.; Kang, Y.; Kim, D.; Lee, T.; Park, S.; Lee, K.; Yoo, D.; Liou, K.; Lee, H.; Sohng, J.; Kim, B.
One-pot enzymatic synthesis of deoxy-thymidine-diphosphate (TDP)-2-deoxy-alpha-D-glucose using phosphomannomutase
J. Mol. Catal. B
62
282-287
2010
Escherichia coli K-12
-
brenda
Higashidani, A.; Bode, L.; Nishikawa, A.; Freeze, H.H.
Exogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts
Mol. Genet. Metab.
96
268-272
2009
Homo sapiens, Mus musculus
brenda
Yu, C.; Li, Y.; Li, B.; Liu, X.; Hao, L.; Chen, J.; Qian, W.; Li, S.; Wang, G.; Bai, S.; Ye, H.; Qin, H.; Shen, Q.; Chen, L.; Zhang, A.; Wang, D.
Molecular analysis of phosphomannomutase (PMM) genes reveals a unique PMM duplication event in diverse Triticeae species and the main PMM isozymes in bread wheat tissues
BMC Plant Biol.
10
214
2010
Hordeum vulgare, Oryza sativa, Triticum turgidum subsp. durum, Triticum turgidum subsp. durum (C8CK11), Triticum turgidum subsp. durum (C8CK12), Triticum turgidum subsp. durum (C8CK13), Triticum urartu, Brachypodium distachyon, Triticum aestivum (C8CK06), Triticum aestivum (C8CK09), Triticum aestivum (C8CK10), Triticum aestivum, Aegilops tauschii (C8CK15), Aegilops tauschii (C8CK16)
brenda
Mitra, S.; Cui, J.; Robbins, P.W.; Samuelson, J.
A deeply divergent phosphoglucomutase (PGM) of Giardia lamblia has both PGM and phosphomannomutase activities
Glycobiology
20
1233-1240
2010
Giardia intestinalis
brenda
Vega, A.I.; Perez-Cerda, C.; Abia, D.; Gamez, A.; Briones, P.; Artuch, R.; Desviat, L.R.; Ugarte, M.; Perez, B.
Expression analysis revealing destabilizing mutations in phosphomannomutase 2 deficiency (PMM2-CDG): Expression analysis of PMM2-CDG mutations
J. Inherit. Metab. Dis.
34
929-939
2011
Homo sapiens (O15305), Homo sapiens
brenda
Chu, H.Y.; Zheng, Q.C.; Li, X.; Zhao, Y.S.; Zhang, J.L.; Zhang, H.X.
DFT investigation on the reaction mechanism catalyzed by alpha-phosphomannomutase1 in protonated/deprotonated states
J. Mol. Model.
17
577-585
2011
Homo sapiens (Q92871)
brenda
Huang, H.; Li, X.; Wu, M.; Wang, S.; Li, G.; Ma, T.
Cloning, expression and characterization of a phosphoglucomutase/phosphomannomutase from sphingan-producing Sphingomonas sanxanigenens
Biotechnol. Lett.
35
1265-1270
2013
Sphingomonas sanxanigenens (M1T754), Sphingomonas sanxanigenens, Sphingomonas sanxanigenens NX02 (M1T754)
brenda
Lee, Y.; Villar, M.T.; Artigues, A.; Beamer, L.J.
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase
J. Biol. Chem.
289
4674-4682
2014
Pseudomonas aeruginosa
brenda
Bandini, G.; Marino, K.; Guether, M.L.; Wernimont, A.K.; Kuettel, S.; Qiu, W.; Afzal, S.; Kelner, A.; Hui, R.; Ferguson, M.A.
Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase
Mol. Microbiol.
85
513-534
2012
Trypanosoma brucei (F4NCC2), Trypanosoma brucei, Trypanosoma brucei 427 (F4NCC2)
brenda
Ji, T.; Zhang, C.; Zheng, L.; Dunaway-Mariano, D.; Allen, K.N.
Structural basis of the molecular switch between phosphatase and mutase functions of human phosphomannomutase 1 under ischemic conditions
Biochemistry
57
3480-3492
2018
Homo sapiens (O15305), Homo sapiens
brenda
Andreotti, G.; Cabeza de Vaca, I.; Poziello, A.; Monti, M.C.; Guallar, V.; Cubellis, M.V.
Conformational response to ligand binding in phosphomannomutase2 insights into inborn glycosylation disorder
J. Biol. Chem.
289
34900-34910
2014
Homo sapiens (O15305), Homo sapiens
brenda
Oh, R.; Moon, S.; Cho, H.; Jang, W.; Kim, J.; Lee, J.; Kong, I.
Cloning and characterization of phosphomannomutase/phosphoglucomutase (pmm/pgm) gene of Vibrio anguillarum related to synthesis of LPS
Microbiol. Biotechnol. Lett.
44
355-362
2016
Vibrio anguillarum, Vibrio anguillarum O1
-
brenda
Kaur, T.; Ghosh, M.
Characterization and upregulation of bifunctional phosphoglucomutase/phosphomannomutase enzyme in an exobiopolymer overproducing strain of Acinetobacter haemolyticus
Microbiol. Res.
181
8-14
2015
Acinetobacter haemolyticus
brenda
Andreotti, G.; Monti, M.C.; Citro, V.; Cubellis, M.V.
Heterodimerization of two pathological mutants enhances the activity of human phosphomannomutase2
PLoS ONE
10
e0139882
2015
Homo sapiens (O15305), Homo sapiens
brenda
Citro, V.; Cimmaruta, C.; Liguori, L.; Viscido, G.; Cubellis, M.V.; Andreotti, G.
A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP Possible implications for the disease PMM2-CDG
PLoS ONE
12
e0189629
2017
Homo sapiens (O15305), Homo sapiens (Q92871), Homo sapiens
brenda
He, C.; Zeng, S.; Teixeira da Silva, J.A.; Yu, Z.; Tan, J.; Duan, J.
Molecular cloning and functional analysis of the phosphomannomutase (PMM) gene from Dendrobium officinale and evidence for the involvement of an abiotic stress response during germination
Protoplasma
254
1693-1704
2017
Dendrobium officinale (A0A0U1WZ18), Dendrobium officinale
brenda
Xu, J.; Sarma, A.V.S.; Wei, Y.; Beamer, L.J.; Van Doren, S.R.
Multiple ligand-bound states of a phosphohexomutase revealed by principal component analysis of NMR peak shifts
Sci. Rep.
7
5343
2017
Pseudomonas aeruginosa (P26276)
brenda
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